ID   CATV_NPVHC              Reviewed;         324 AA.
AC   Q9WGE0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Viral cathepsin;
DE            Short=V-cath;
DE            EC=3.4.22.50;
DE   AltName: Full=Cysteine proteinase;
DE            Short=CP;
DE   Flags: Precursor;
GN   Name=VCATH;
OS   Hyphantria cunea nuclear polyhedrosis virus (HcNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=28288;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gong C., Kobayashi J., Miyajima N., Zhang C., Jin W., Wu X.;
RT   "The nucleotide sequence of Hyphantria cunea nuclear polyhedrosis virus
RT   cysteine protease gene.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cysteine protease that plays an essential role in host
CC       liquefaction to facilitate horizontal transmission of the virus. May
CC       participate in the degradation of foreign protein expressed by the
CC       baculovirus system (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase of broad specificity, hydrolyzing substrates of
CC         both cathepsin L and cathepsin B.; EC=3.4.22.50;
CC   -!- PTM: Synthesized as an inactive proenzyme and activated by proteolytic
CC       removal of the inhibitory propeptide. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AF120926; AAD31760.1; -; Genomic_DNA.
DR   SMR; Q9WGE0; -.
DR   MEROPS; C01.083; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000322210"
FT   CHAIN           114..324
FT                   /note="Viral cathepsin"
FT                   /id="PRO_0000050580"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        134..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        168..208
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..311
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36966 MW;  525B179F3D80FABD CRC64;
     MNKIVLCLLV FCVAHSAAYD LLKAPSYFED FLHKFNKHYS SESEKLRRFQ IFQHNLEEII
     IKNQNDTTAQ YEINKFSDLS KDETISKYTG LALPLQTQNF CEVVVLNRPP DKGPLEFDWR
     RLNKVTSVKN QGICGACWAF ATLASLESQF AIKHNQLINL SEQQLIDCDY VDAGCNGGLL
     HTAYEAVMQM GGVQAENDYP YEGSDGNCRV DVAKFVVKVK KCYRYIAVFE EKLKDLLRIV
     GPIPVAIDAS DIVNYRRGIM RYCSNYGFNH AVLLVGYGVE NNVPYWILKN TWGEDWGEQG
     YFRVQQNINA CGIRNELLAS AEIY